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TitleMechanism of Crosstalk between the LSD1 Demethylase and HDAC1 Deacetylase in the CoREST Complex.
Journal, issue, pagesCell Rep, Vol. 30, Issue 8, Page 2699-22711.e8, Year 2020
Publish dateFeb 25, 2020
AuthorsYun Song / Lisbeth Dagil / Louise Fairall / Naomi Robertson / Mingxuan Wu / T J Ragan / Christos G Savva / Almutasem Saleh / Nobuhiro Morone / Micha B A Kunze / Andrew G Jamieson / Philip A Cole / D Flemming Hansen / John W R Schwabe /
PubMed AbstractThe transcriptional corepressor complex CoREST is one of seven histone deacetylase complexes that regulate the genome through controlling chromatin acetylation. The CoREST complex is unique in ...The transcriptional corepressor complex CoREST is one of seven histone deacetylase complexes that regulate the genome through controlling chromatin acetylation. The CoREST complex is unique in containing both histone demethylase and deacetylase enzymes, LSD1 and HDAC1, held together by the RCOR1 scaffold protein. To date, it has been assumed that the enzymes function independently within the complex. Now, we report the assembly of the ternary complex. Using both structural and functional studies, we show that the activity of the two enzymes is closely coupled and that the complex can exist in at least two distinct states with different kinetics. Electron microscopy of the complex reveals a bi-lobed structure with LSD1 and HDAC1 enzymes at opposite ends of the complex. The structure of CoREST in complex with a nucleosome reveals a mode of chromatin engagement that contrasts with previous models.
External linksCell Rep / PubMed:32101746 / PubMed Central
MethodsEM (single particle)
Resolution17.5 - 26.1 Å
Structure data

EMDB-10626:
Negative stain map of CoREST complex (LSD1:RCOR1:HDAC1)
Method: EM (single particle) / Resolution: 17.5 Å

EMDB-10627:
Cryo-EM map of glutaraldehye cross-linked CoREST complex (LSD1:RCOR1:HDAC1)
Method: EM (single particle) / Resolution: 17.5 Å

EMDB-10628:
Cryo EM map of BS3 crosslinked CoREST complex (LSD1:RCOR1:HDAC1)- closed form
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-10629:
Cryo EM map of BS3 crosslinked CoREST complex (LSD1:RCOR1:HDAC1) - open form
Method: EM (single particle) / Resolution: 21.5 Å

EMDB-10630:
Interaction of the CoREST complex with a nucleosome with 185 bp 601 sequence DNA and a propargylamine mimic of dimethy Lys4 histone H3
Method: EM (single particle) / Resolution: 26.1 Å

Source
  • Homo sapiens (human)

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